COFE_METJA
ID COFE_METJA Reviewed; 249 AA.
AC Q58178;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Coenzyme F420:L-glutamate ligase;
DE EC=6.3.2.31;
DE EC=6.3.2.34;
DE AltName: Full=Coenzyme F420-0:L-glutamate ligase;
DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase;
DE AltName: Full=F420:glutamyl ligase;
GN Name=cofE; OrderedLocusNames=MJ0768;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=12911320; DOI=10.1021/bi034779b;
RA Li H., Graupner M., Xu H., White R.H.;
RT "CofE catalyzes the addition of two glutamates to F420-0 in F420 coenzyme
RT biosynthesis in Methanococcus jannaschii.";
RL Biochemistry 42:9771-9778(2003).
CC -!- FUNCTION: Catalyzes the GTP-dependent successive addition of two L-
CC glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-
CC 5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate
CC (F420-2), with a gamma-linkage between the two glutamates. Cannot use
CC F420-2 as substrate to add more glutamates. Exhibits maximum activity
CC with GTP, compared with UTP (66%) and dGTP (25%); with ATP, only F420-1
CC is observed as the product; CTP and TTP support no activity.
CC {ECO:0000269|PubMed:12911320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) +
CC oxidized coenzyme F420-1 + phosphate; Xref=Rhea:RHEA:30555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:59907,
CC ChEBI:CHEBI:59920; EC=6.3.2.31;
CC Evidence={ECO:0000269|PubMed:12911320};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) +
CC oxidized coenzyme F420-2 + phosphate; Xref=Rhea:RHEA:30523,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57922, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:59920; EC=6.3.2.34;
CC Evidence={ECO:0000269|PubMed:12911320};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12911320};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12911320};
CC Note=Binds 2 divalent metal cations per subunit. The ions could be
CC magnesium and/or manganese. {ECO:0000269|PubMed:12911320};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:12911320};
CC Note=Monovalent cation. The ion could be potassium.
CC {ECO:0000269|PubMed:12911320};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for F420-0 {ECO:0000269|PubMed:12911320};
CC KM=0.21 uM for F420-1 {ECO:0000269|PubMed:12911320};
CC Vmax=2.4 nmol/min/mg enzyme with F420-0 as substrate
CC {ECO:0000269|PubMed:12911320};
CC Vmax=0.96 nmol/min/mg enzyme with F420-1 as substrate
CC {ECO:0000269|PubMed:12911320};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:12911320};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Thermostable. Retains 70%
CC of its activity after heating at 80 degrees Celsius for 15 minutes.
CC {ECO:0000269|PubMed:12911320};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12911320}.
CC -!- SIMILARITY: Belongs to the CofE family. {ECO:0000305}.
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DR EMBL; L77117; AAB98763.1; -; Genomic_DNA.
DR PIR; H64395; H64395.
DR RefSeq; WP_010870273.1; NC_000909.1.
DR AlphaFoldDB; Q58178; -.
DR SMR; Q58178; -.
DR STRING; 243232.MJ_0768; -.
DR EnsemblBacteria; AAB98763; AAB98763; MJ_0768.
DR GeneID; 1451645; -.
DR KEGG; mja:MJ_0768; -.
DR eggNOG; arCOG02714; Archaea.
DR HOGENOM; CLU_051152_1_1_2; -.
DR InParanoid; Q58178; -.
DR OMA; KHGFVCA; -.
DR OrthoDB; 73785at2157; -.
DR PhylomeDB; Q58178; -.
DR BioCyc; MetaCyc:MON-12187; -.
DR BRENDA; 6.3.2.31; 3260.
DR BRENDA; 6.3.2.34; 3260.
DR SABIO-RK; Q58178; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity; IDA:MENGO.
DR GO; GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01258; F420_ligase_CofE; 1.
DR InterPro; IPR008225; F420-0_g-glutamyl_ligase.
DR InterPro; IPR002847; F420-0_gamma-glut_ligase-dom.
DR InterPro; IPR023659; F420_ligase_CofE_arc.
DR Pfam; PF01996; F420_ligase; 1.
DR TIGRFAMs; TIGR01916; F420_cofE; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome.
FT CHAIN 1..249
FT /note="Coenzyme F420:L-glutamate ligase"
FT /id="PRO_0000145789"
FT BINDING 15..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 45..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 211..218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 249 AA; 27148 MW; A6B66FF4B52C15A2 CRC64;
MIKEKRKVEV IGLELPIFKG GEQINLSELI AQYPIEDGDI IVIAETLISK LEGGVIDRDK
IIPSKEAIEL AKKTGKDPKV VQVILDEAKE IVKVGKNFII TETKHGFVCA NSGVDESNIY
KGIKILPKNP DESAEKIRKE IEKLTGKRVG VIISDSVGRP FRKGAVGIAI GVSGILALWD
RKGEKDLFGR ELKTTEVAIA DELASMANVV MGEADEGIPV VIIRGANVPF GNGKGRDLIR
PKEEDVFRN
